{"refrec":{"BRefID":289173,"RR":"<b>Richter, S.; Helm, C.; Meunier, F.A.; Hering, L.; Campbell, L.I.; Drukewitz, S.H.; Undheim, E.A.B.; Jenner, R.A.; Schiavo, G.; Bleidorn, C.</b> (2017). Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system. <i>BMC Evol. Biol. 17</i>. <a href=\"https://dx.doi.org/10.1186/s12862-017-0904-4\" target=\"_blank\">https://dx.doi.org/10.1186/s12862-017-0904-4</a>","BEntID":281210,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":null,"RefStringPartII":". <i>BMC Evol. Biol. 17</i>. <a href=\"https://dx.doi.org/10.1186/s12862-017-0904-4\" target=\"_blank\">https://dx.doi.org/10.1186/s12862-017-0904-4</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Richter, S.; Helm, C.; Meunier, F.A.; Hering, L.; Campbell, L.I.; Drukewitz, S.H.; Undheim, E.A.B.; Jenner, R.A.; Schiavo, G.; Bleidorn, C.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Richter, S. <i>et al.</i>","Englishabstract":"BackgroundWe present the first molecular characterization of glycerotoxin (GLTx), a potent neurotoxin found in the venom of the bloodworm <i>Glycera tridactyla</i> (Glyceridae, Annelida). Within the animal kingdom, GLTx shows a unique mode of action as it can specifically up-regulate the activity of Ca<sub>v</sub>2.2 channels (N-type) in a reversible manner. The lack of sequence information has so far hampered a detailed understanding of its mode of action.ResultsOur analyses reveal three ~3.8 kb GLTx full-length transcripts, show that GLTx represents a multigene family, and suggest it functions as a dimer. An integrative approach using transcriptomics, quantitative real-time PCR, <i>in situ</i> hybridization, and immunocytochemistry shows that GLTx is highly expressed exclusively in four pharyngeal lobes, a previously unrecognized part of the venom apparatus.ConclusionsOur results overturn a century old textbook view on the glycerid venom system, suggesting that it is anatomically and functionally much more complex than previously thought. The herein presented GLTx sequence information constitutes an important step towards the establishment of GLTx as a versatile tool to understand the mechanism of synaptic function, as well as the mode of action of this novel neurotoxin.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-11 01:32:20.148053","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Annelida; Glyceridae; Calcium channel; Neurotoxin; GLTx; Venom system","OtherDescriptors":null,"Notes":null,"AnaPub":2017,"MonPub":null,"DateUpdate":"2017-09-19","DateCreate":"2017-09-18","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000397336600001","VABBcode":null,"OpenAcc":1,"DOI":"10.1186/s12862-017-0904-4"},"refs":null,"anarec":{"AnaID":289173,"PubliDate":2017,"Pagination":null,"XtraPublOfAnaID":null,"ISBN":null,"Volume":"17","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":136230,"SerRR":"BMC Evolutionary Biology. 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